Function of human Rh based on structure of RhCG at 2.1 Å
Function of human Rh based on structure of RhCG at 2.1 Å
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DOI：
10.1073/pnas.1003587107
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发表时间：
2010-05-25
影响因子：
11.1
通讯作者：
Stroud, Robert M.
中科院分区：
文献类型：
--
作者：
Gruswitz, Franz;Chaudhary, Sarika;Stroud, Robert M.
在人类中，Rh（恒河猴）蛋白质家族促进了NH3穿过细胞膜的运输。人Rh C糖蛋白（RhCG）形成三聚体复合物，在氨排泄和肾脏pH调节中起重要作用。在2.1埃分辨率下测定的人RhCG的X射线晶体结构揭示了氨转运的机制。每个单体含有12个跨膜螺旋，比细菌同系物多一个。重组成脂蛋白体，RhCG进行NH3，以提高内部pH值。模型的红细胞Rh复合物的基础上，我们的RhCG结构表明，红细胞Rh复合物是由随机组装的异源三聚体的RhAG，RhD，和RhCE。
In humans, NH3 transport across cell membranes is facilitated by the Rh (rhesus) family of proteins. Human Rh C glycoprotein (RhCG) forms a trimeric complex that plays an essential role in ammonia excretion and renal pH regulation. The X-ray crystallographic structure of human RhCG, determined at 2.1 angstrom resolution, reveals the mechanism of ammonia transport. Each monomer contains 12 transmembrane helices, one more than in the bacterial homologs. Reconstituted into proteoliposomes, RhCG conducts NH3 to raise internal pH. Models of the erythrocyte Rh complex based on our RhCG structure suggest that the erythrocytic Rh complex is composed of stochastically assembled heterotrimers of RhAG, RhD, and RhCE.